Re- or displacement of invariant residues in the C-terminal half of the catalytic domain strongly affects catalysis by glucosyltransferase R

It is shown that exchanges of single invariant amino acids in two C-terminal catalytic domain segments of the glucosyltransferase R (GtfR) strongly affect its catalytic properties. Drastic decreases of activity through re- or displacements of Tyr965 demonstrate a crucial role of this residue. Simila...

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Bibliographic Details
Published in:FEBS letters 2008-02, Vol.582 (4), p.491-496
Main Authors: Wittrock, Sabine, Swistowska, Anna Maria, Collisi, Wera, Hofmann, Birgit, Hecht, Hans-Jürgen, Hofer, Bernd
Format: Article
Language:English
Subjects:
amino acid
Catalysis
Catalytic determinants
Catalytic Domain
Enzyme variant
Fru
fructose
Glc
Glucansucrase
glucose
Glucosyltransferase
Glycosyltransferases - chemistry
Glycosyltransferases - metabolism
GTF
Kinetics
Models, Molecular
Permutation hypothesis
Suc
sucrose
Three-dimensional structure
wild-type
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Summary:It is shown that exchanges of single invariant amino acids in two C-terminal catalytic domain segments of the glucosyltransferase R (GtfR) strongly affect its catalytic properties. Drastic decreases of activity through re- or displacements of Tyr965 demonstrate a crucial role of this residue. Similarly, exchanges of amino acids Asp1004, Val1006, and Tyr1011 profoundly influenced catalytic parameters. These results are interpreted on the basis of a homology model of the catalytic domain. They are consistent with the view that Tyr965 is a constituent of the substrate-binding pocket and directly contacts the sucrose molecule, whereas the other critical residues contribute to the required positioning of Tyr965 and other active site residues.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.12.040